ID A0A1H9W1R3_9BACI Unreviewed; 327 AA.
AC A0A1H9W1R3;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 16.
DE RecName: Full=Peptide chain release factor 2 {ECO:0000256|ARBA:ARBA00019192, ECO:0000256|HAMAP-Rule:MF_00094};
DE Short=RF-2 {ECO:0000256|HAMAP-Rule:MF_00094};
GN Name=prfB {ECO:0000256|HAMAP-Rule:MF_00094};
GN ORFNames=SAMN05444126_12635 {ECO:0000313|EMBL:SES27845.1};
OS Salisediminibacterium haloalkalitolerans.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae;
OC Salisediminibacterium.
OX NCBI_TaxID=1464123 {ECO:0000313|EMBL:SES27845.1, ECO:0000313|Proteomes:UP000199318};
RN [1] {ECO:0000313|EMBL:SES27845.1, ECO:0000313|Proteomes:UP000199318}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=10nlg {ECO:0000313|EMBL:SES27845.1,
RC ECO:0000313|Proteomes:UP000199318};
RA de Groot N.N.;
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Peptide chain release factor 2 directs the termination of
CC translation in response to the peptide chain termination codons UGA and
CC UAA. {ECO:0000256|ARBA:ARBA00002613, ECO:0000256|HAMAP-Rule:MF_00094}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00094}.
CC -!- PTM: Methylated by PrmC. Methylation increases the termination
CC efficiency of RF2. {ECO:0000256|HAMAP-Rule:MF_00094}.
CC -!- SIMILARITY: Belongs to the prokaryotic/mitochondrial release factor
CC family. {ECO:0000256|ARBA:ARBA00010835, ECO:0000256|HAMAP-
CC Rule:MF_00094}.
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DR EMBL; FOGV01000026; SES27845.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1H9W1R3; -.
DR STRING; 1464123.SAMN05444126_12635; -.
DR Proteomes; UP000199318; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0016149; F:translation release factor activity, codon specific; IEA:UniProtKB-UniRule.
DR Gene3D; 3.30.160.20; -; 1.
DR Gene3D; 3.30.70.1660; -; 1.
DR Gene3D; 1.20.58.410; Release factor; 1.
DR HAMAP; MF_00094; Rel_fac_2; 1.
DR InterPro; IPR005139; PCRF.
DR InterPro; IPR000352; Pep_chain_release_fac_I.
DR InterPro; IPR045853; Pep_chain_release_fac_I_sf.
DR InterPro; IPR004374; PrfB.
DR NCBIfam; TIGR00020; prfB; 1.
DR PANTHER; PTHR43116; PEPTIDE CHAIN RELEASE FACTOR 2; 1.
DR PANTHER; PTHR43116:SF3; RF_PROK_I DOMAIN-CONTAINING PROTEIN; 1.
DR Pfam; PF03462; PCRF; 1.
DR Pfam; PF00472; RF-1; 1.
DR SMART; SM00937; PCRF; 1.
DR SUPFAM; SSF75620; Release factor; 1.
DR PROSITE; PS00745; RF_PROK_I; 1.
PE 3: Inferred from homology;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00094};
KW Methylation {ECO:0000256|ARBA:ARBA00022481, ECO:0000256|HAMAP-
KW Rule:MF_00094}; Protein biosynthesis {ECO:0000256|HAMAP-Rule:MF_00094};
KW Reference proteome {ECO:0000313|Proteomes:UP000199318}.
FT DOMAIN 205..221
FT /note="Prokaryotic-type class I peptide chain release
FT factors"
FT /evidence="ECO:0000259|PROSITE:PS00745"
FT COILED 16..76
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 234..273
FT /evidence="ECO:0000256|SAM:Coils"
FT MOD_RES 212
FT /note="N5-methylglutamine"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00094"
SQ SEQUENCE 327 AA; 36989 MW; 45D000D25A55504A CRC64;
MATPSFWDDQ TEAQKVIGET NALKEMTQTY RKLEEELENL EISFQLVEEE GDEELAAEME
AQLKTLIKEV NAFELQLLLS GPYDKNNAIL EIHPGAGGTE SQDWASMLLR MYTRFAESMN
FQVDTLDYLP GDEAGVKSVV LQISGPNAYG YLKAEKGVHR LVRISPFDSS GRRHTSFASC
EVMPELDDNV EVTINSDDLR IDTFRSSGAG GQHVNTTDSA VRITHLPTNT VVSCQSERSQ
LKNREKAMKA LRSKLHQLEL QKQQEEADEI RGEQSDIGWG SQIRSYVFHP YNMVKDHRTN
YEVGNTEAVM DGKLMPFIDA YLRKQIE
//